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Conserved domains on  [gi|492484521|ref|WP_005861219|]
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MULTISPECIES: fumarylacetoacetate hydrolase family protein [Parabacteroides]

Protein Classification

fumarylacetoacetate hydrolase family protein( domain architecture ID 11415096)

fumarylacetoacetate (FAA) hydrolase family protein belongs to the FAA hydrolase family which includes a large variety of metabolic enzymes, including those with hydrolase functions involved in the breakdown of aromatic compounds, oxaloacetate decarboxylase, and enzymes associated with other catabolic pathways including decarboxylation of substrates other than oxaloacetate, hydration, isomerization and hydroxylation reactions

CATH:  2.30.30.370
Gene Ontology:  GO:0003824|GO:0016787
PubMed:  29487229
SCOP:  4002580

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
2-190 4.78e-75

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 439949  Cd Length: 206  Bit Score: 224.56  E-value: 4.78e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   2 KIIAVGMNYAAHNKELHHSLElSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRY---Y 78
Cdd:COG0179    7 KIICVGLNYADHAAEMGNDVP-EEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHvagY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  79 nevTVGIDFTARDLQnklRAQGLPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKII 157
Cdd:COG0179   86 ---TVANDVTARDLQ---RERGGQWTRGKSFDTFCPLGPWIvTADEIPDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELI 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 492484521 158 AYVSRFFTLKIGDLIYTGTPAGVGPVKIDDHLE 190
Cdd:COG0179  160 AYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVE 192
 
Name Accession Description Interval E-value
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
2-190 4.78e-75

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 439949  Cd Length: 206  Bit Score: 224.56  E-value: 4.78e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   2 KIIAVGMNYAAHNKELHHSLElSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRY---Y 78
Cdd:COG0179    7 KIICVGLNYADHAAEMGNDVP-EEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHvagY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  79 nevTVGIDFTARDLQnklRAQGLPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKII 157
Cdd:COG0179   86 ---TVANDVTARDLQ---RERGGQWTRGKSFDTFCPLGPWIvTADEIPDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELI 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 492484521 158 AYVSRFFTLKIGDLIYTGTPAGVGPVKIDDHLE 190
Cdd:COG0179  160 AYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVE 192
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
2-198 1.27e-52

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 167.96  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   2 KIIAVGMNYAAHNKELHhSLELSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYNEV 81
Cdd:PRK10691  18 KVVCVGSNYAKHIKEMG-SATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  82 TVGIDFTARDLQNKLRAQGLPWEISKAFDNSAVIGTFIPL-EQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAYV 160
Cdd:PRK10691  97 GVALDLTLRDLQGKMKKAGQPWEKAKAFDNSCPISGFIPVaEFTGDPQNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYM 176
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492484521 161 SRFFTLKIGDLIYTGTPAGVGPVKIDDHLEGYLGERKL 198
Cdd:PRK10691 177 SRFFTLRAGDVVLTGTPEGVGPLQSGDELTVTFNGHSL 214
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
4-181 2.28e-48

Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerizes this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.


Pssm-ID: 460252  Cd Length: 210  Bit Score: 157.06  E-value: 2.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521    4 IAVGMNYAAHNKELHHSLELSEP----TIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYN 79
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAEPVPDFpiplVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALDYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   80 EVTVGIDFTARDLQnkLRAQGLPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIA 158
Cdd:pfam01557  81 GYTLANDVSARDLQ--RREMPLQWFRGKSFDGFTPLGPWIvTRDELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELIA 158
                         170       180
                  ....*....|....*....|...
gi 492484521  159 YVSRFFTLKIGDLIYTGTPAGVG 181
Cdd:pfam01557 159 HLSQFMTLRPGDIILTGTPSGVG 181
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
2-190 7.68e-33

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131356 [Multi-domain]  Cd Length: 245  Bit Score: 117.99  E-value: 7.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521    2 KIIAVGMNYAAHNKELHHSLElSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYNEV 81
Cdd:TIGR02303  44 TIFALGLNYADHASELGFSPP-EEPLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGY 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   82 TVGIDFTARD-LQNKLRaqglPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAY 159
Cdd:TIGR02303 123 TIANDYAIRDyLENYYR----PNLRVKNRDTFTPIGPWIvDKEDVEDPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEY 198
                         170       180       190
                  ....*....|....*....|....*....|.
gi 492484521  160 VSRFFTLKIGDLIYTGTPAGVGPVKIDDHLE 190
Cdd:TIGR02303 199 LSEFMTLEPGDVILTGTPKGLSDVKPGDVVR 229
 
Name Accession Description Interval E-value
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
2-190 4.78e-75

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 439949  Cd Length: 206  Bit Score: 224.56  E-value: 4.78e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   2 KIIAVGMNYAAHNKELHHSLElSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRY---Y 78
Cdd:COG0179    7 KIICVGLNYADHAAEMGNDVP-EEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHvagY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  79 nevTVGIDFTARDLQnklRAQGLPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKII 157
Cdd:COG0179   86 ---TVANDVTARDLQ---RERGGQWTRGKSFDTFCPLGPWIvTADEIPDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELI 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 492484521 158 AYVSRFFTLKIGDLIYTGTPAGVGPVKIDDHLE 190
Cdd:COG0179  160 AYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVE 192
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
2-198 1.27e-52

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 167.96  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   2 KIIAVGMNYAAHNKELHhSLELSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYNEV 81
Cdd:PRK10691  18 KVVCVGSNYAKHIKEMG-SATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  82 TVGIDFTARDLQNKLRAQGLPWEISKAFDNSAVIGTFIPL-EQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAYV 160
Cdd:PRK10691  97 GVALDLTLRDLQGKMKKAGQPWEKAKAFDNSCPISGFIPVaEFTGDPQNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYM 176
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492484521 161 SRFFTLKIGDLIYTGTPAGVGPVKIDDHLEGYLGERKL 198
Cdd:PRK10691 177 SRFFTLRAGDVVLTGTPEGVGPLQSGDELTVTFNGHSL 214
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
4-181 2.28e-48

Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerizes this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.


Pssm-ID: 460252  Cd Length: 210  Bit Score: 157.06  E-value: 2.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521    4 IAVGMNYAAHNKELHHSLELSEP----TIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYN 79
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAEPVPDFpiplVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALDYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   80 EVTVGIDFTARDLQnkLRAQGLPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIA 158
Cdd:pfam01557  81 GYTLANDVSARDLQ--RREMPLQWFRGKSFDGFTPLGPWIvTRDELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELIA 158
                         170       180
                  ....*....|....*....|...
gi 492484521  159 YVSRFFTLKIGDLIYTGTPAGVG 181
Cdd:pfam01557 159 HLSQFMTLRPGDIILTGTPSGVG 181
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
2-190 7.68e-33

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131356 [Multi-domain]  Cd Length: 245  Bit Score: 117.99  E-value: 7.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521    2 KIIAVGMNYAAHNKELHHSLElSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYNEV 81
Cdd:TIGR02303  44 TIFALGLNYADHASELGFSPP-EEPLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGY 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   82 TVGIDFTARD-LQNKLRaqglPWEISKAFDNSAVIGTFI-PLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAY 159
Cdd:TIGR02303 123 TIANDYAIRDyLENYYR----PNLRVKNRDTFTPIGPWIvDKEDVEDPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEY 198
                         170       180       190
                  ....*....|....*....|....*....|.
gi 492484521  160 VSRFFTLKIGDLIYTGTPAGVGPVKIDDHLE 190
Cdd:TIGR02303 199 LSEFMTLEPGDVILTGTPKGLSDVKPGDVVR 229
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
3-183 6.68e-29

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 111.30  E-value: 6.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   3 IIAVGMNYAAHNKELHHSLElSEPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYNEVT 82
Cdd:PRK15203 225 LFALGLNYADHASELEFKPP-EEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARKVSEADAMDYVAGYT 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  83 VGIDFTARD-LQNKLRaqglPWEISKAFDNSAVIG-TFIPLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAYV 160
Cdd:PRK15203 304 VCNDYAIRDyLENYYR----PNLRVKSRDGLTPILsTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYL 379
                        170       180
                 ....*....|....*....|...
gi 492484521 161 SRFFTLKIGDLIYTGTPAGVGPV 183
Cdd:PRK15203 380 SEFMTLNPGDMIATGTPKGLSDV 402
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
2-185 8.07e-18

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related C-terminal domain (TIGR02303). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131358  Cd Length: 205  Bit Score: 77.85  E-value: 8.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521    2 KIIAVGMNYAAHNKELHHSLELS-------EPTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFA 74
Cdd:TIGR02305   2 TVFGVALNYREQLDRLQEAFQQApykappkTPVLYIKPRNTHNGCGQPIPLPAGVEKLRSGATLALVVGRTACRVREEEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   75 HRYYNEVTVGIDFTardlqnklraqgLPWEI-------SKAFDNSAVIGTFIPLEQAGDVNRLPFHLDINGSKVQEGNTS 147
Cdd:TIGR02305  82 LDYVAGYALVNDVS------------LPEDSyyrpaikAKCRDGFCPIGPEVPLSAIGNPDELTIYTYINGKPAQSNNTS 149
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 492484521  148 NMLFSVDKIIAYVSRFFTLKIGDLIYTGTPagVGPVKI 185
Cdd:TIGR02305 150 NLVRSAAQLISELSEFMTLNPGDVLLLGTP--EARVEV 185
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
2-190 3.37e-17

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 79.03  E-value: 3.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521   2 KIIAVGMNYAAHNKELHHSLELsePTIFMKSDSSLLKDGKPFFIPDFSSEVHYETEIVVRIDRLGKNIAERFAHRYYNEV 81
Cdd:PRK12764  23 KVIAVHLNYPSRAAQRGRTPAQ--PSYFLKPSSSLALSGGTVERPAGTELLAFEGEIALVIGRPARRVSPEDAWSHVAAV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492484521  82 TVGIDFTARDLQNKLRAQGLPweiSKAFDNSAVIGTFIPLEQAGDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAYVS 161
Cdd:PRK12764 101 TAANDLGVYDLRYADKGSNLR---SKGGDGFTPIGPALISARGVDPAQLRVRTWVNGELVQDDTTEDLLFPFAQLVADLS 177
                        170       180
                 ....*....|....*....|....*....
gi 492484521 162 RFFTLKIGDLIYTGTPAGVGPVKIDDHLE 190
Cdd:PRK12764 178 QLLTLEEGDVILTGTPAGSSVAAPGDVVE 206
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
106-177 2.00e-04

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 41.19  E-value: 2.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492484521 106 SKAFDNSAVIGTFIPLEqagDVNRLPFHLDINGSKVQEGNTSNMLFSVDKIIAYVSRFFTLKIGDLIYTGTP 177
Cdd:PRK15203 109 AKCRDGFCPIGETVALS---NVDNLTIYTEINGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGTP 177
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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